MolNFT v1 · #98907 · protein
Structure of escherichia COLI threonine aldolase in complex with serine
4LNM · Low-specificity L-threonine aldolase: “Structure of escherichia COLI threonine aldolase in complex with serine”. X-ray diffraction, 3 ligands (PLG, PLR, CA), 3 pockets (best druggability 0.63). MolNFT v1 #98907 on GenesisL1: 3D…
- PDB
- 4LNM
- Type
- protein
- Length
- 662 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low-specificity L-threonine aldolase
- EC
- 4.1.2.5
- UniProt
- E7U392
- Ligands
- PLG, PLR, CA
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Low-specificity L-threonine aldolase (EC 4.1.2.5) | protein | 331 | 44% helix, 18% strand | E7U392 |
Ligands and binding sites
- PLG · N-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane] · ligand · chains B
- PLR · (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate · ligand · chains A
- CA · Calcium ion · metal · 3 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.63 | 0.77 | 65 | PLR |
| 2 | 250 | 0.53 | 0.76 | 45 | PLG |
| 3 | 50 | 0.40 | 0.82 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 992 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4LNM · Structure of Escherichia coli Threonine Aldolase in Complex with Serine · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt E7U392
- Elsewhere: RCSB PDB 4LNM · PDBe 4LNM · UniProt E7U392
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